Team:Cambridge/References/ProjectBioluminescence/Recovery
From 2010.igem.org
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==CoA== | ==CoA== | ||
*[http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B73G9-47G3TGV-1S9-1&_cdi=11521&_user=1495569&_pii=0006300258903810&_orig=search&_coverDate=12%2F31%2F1958&_sk=999729999&view=c&wchp=dGLbVzz-zSkWA&md5=4420b38ef24aba8ca23e0b8ce2b3a953&ie=/sdarticle.pdf CoA is required to remove oxyluciferin from luciferase] | *[http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B73G9-47G3TGV-1S9-1&_cdi=11521&_user=1495569&_pii=0006300258903810&_orig=search&_coverDate=12%2F31%2F1958&_sk=999729999&view=c&wchp=dGLbVzz-zSkWA&md5=4420b38ef24aba8ca23e0b8ce2b3a953&ie=/sdarticle.pdf CoA is required to remove oxyluciferin from luciferase] | ||
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==D-Cysteine== | ==D-Cysteine== | ||
E. coli growth is impaired in the presence of micromolar amounts of D-cysteine. [http://www.ncbi.nlm.nih.gov/pubmed/11527960 Soutourina et al.] found that E. coli contain a D-cysteine desulfhydrase which can convert D-cysteine into pyruvate, H2S, and NH3. Overexpression of yedO (the E. coli gene encoding D-cysteine desulfydrase activity) protected E. coli against D-cysteine, whereas its inactivation rendered E. coli hypersensitive. With yedO intact, E. coli growth was improved by addition of D-cysteine as the sole sulfur source. | E. coli growth is impaired in the presence of micromolar amounts of D-cysteine. [http://www.ncbi.nlm.nih.gov/pubmed/11527960 Soutourina et al.] found that E. coli contain a D-cysteine desulfhydrase which can convert D-cysteine into pyruvate, H2S, and NH3. Overexpression of yedO (the E. coli gene encoding D-cysteine desulfydrase activity) protected E. coli against D-cysteine, whereas its inactivation rendered E. coli hypersensitive. With yedO intact, E. coli growth was improved by addition of D-cysteine as the sole sulfur source. | ||
Similar to L-cysteine, D-cysteine exerts toxicity through inhibition of threonine deaminase, a key enzyme of the isoleucine, leucine, and valine biosynthesis pathway. Growth protection against D-cysteine in minimal medium was conferred by simultaneous addition of isoleucine, leucine and valine. L-aspartate was also observed to exert a protective effect against D-cysteine toxicity. | Similar to L-cysteine, D-cysteine exerts toxicity through inhibition of threonine deaminase, a key enzyme of the isoleucine, leucine, and valine biosynthesis pathway. Growth protection against D-cysteine in minimal medium was conferred by simultaneous addition of isoleucine, leucine and valine. L-aspartate was also observed to exert a protective effect against D-cysteine toxicity. | ||
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Revision as of 09:22, 26 July 2010
LRE
- Paper on isolation of A-LRE
- A-LRE (P.pyralis) Sequence
- RACE-based amplification of cDNA and expression of a luciferin-regenerating enzyme (LRE): An attempt towards persistent bioluminescent signal
CoA
D-Cysteine
E. coli growth is impaired in the presence of micromolar amounts of D-cysteine. Soutourina et al. found that E. coli contain a D-cysteine desulfhydrase which can convert D-cysteine into pyruvate, H2S, and NH3. Overexpression of yedO (the E. coli gene encoding D-cysteine desulfydrase activity) protected E. coli against D-cysteine, whereas its inactivation rendered E. coli hypersensitive. With yedO intact, E. coli growth was improved by addition of D-cysteine as the sole sulfur source. Similar to L-cysteine, D-cysteine exerts toxicity through inhibition of threonine deaminase, a key enzyme of the isoleucine, leucine, and valine biosynthesis pathway. Growth protection against D-cysteine in minimal medium was conferred by simultaneous addition of isoleucine, leucine and valine. L-aspartate was also observed to exert a protective effect against D-cysteine toxicity.